Anthrax lethal factor endopeptidase
Crystallographic structure of anthrax lethal factor (rainbow colored cartoon, N-terminus = blue, C-terminus = red) complexed with the inhibitor GM6001 (space-filling model, carbon = white, oxygen = red, nitrogen = blue).[1]
Identifiers
EC no.3.4.24.83
CAS no.477950-41-7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

Anthrax lethal factor endopeptidase (EC 3.4.24.83, lethal toxin) is an enzyme that catalyzes the hydrolysis of mitogen-activated protein kinase kinases. This enzyme is a component of the lethal factor produced by the bacterium Bacillus anthracis. The preferred cleavage site can be denoted by BBBBxHxH, in which B denotes a basic amino acid Arg or Lys, H denotes a hydrophobic amino acid, and x is any amino acid.[2]

References

  1. PDB: 1PWU; Turk BE, Wong TY, Schwarzenbacher R, Jarrell ET, Leppla SH, Collier RJ, Liddington RC, Cantley LC (January 2004). "The structural basis for substrate and inhibitor selectivity of the anthrax lethal factor". Nat. Struct. Mol. Biol. 11 (1): 60–6. doi:10.1038/nsmb708. PMID 14718924. S2CID 39119275.
  2. Pannifer AD, Wong TY, Schwarzenbacher R, Renatus M, Petosa C, Bienkowska J, Lacy DB, Collier RJ, Park S, Leppla SH, Hanna P, Liddington RC (November 2001). "Crystal structure of the anthrax lethal factor" (PDF). Nature. 414 (6860): 229–33. doi:10.1038/n35101998. hdl:2027.42/62772. PMID 11700563. S2CID 9212908.


This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.